Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination

Jessica L. Kelliher; Kirk L. West; Qingguo Gong; Justin W. C. Leung

doi:10.1038/s41467-020-16307-4

Nature Communications (May 2020)

Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination

Jessica L. Kelliher,
Kirk L. West,
Qingguo Gong,
Justin W. C. Leung

Affiliations

Jessica L. Kelliher: Department of Radiation Oncology, College of Medicine, University of Arkansas for Medical Sciences
Kirk L. West: Department of Radiation Oncology, College of Medicine, University of Arkansas for Medical Sciences
Qingguo Gong: Hefei National Laboratory for Physical Science at the Microscale, School of Life Sciences, University of Science and Technology of China
Justin W. C. Leung: Department of Radiation Oncology, College of Medicine, University of Arkansas for Medical Sciences

DOI: https://doi.org/10.1038/s41467-020-16307-4
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

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Histone ubiquitination plays a critical role in the DNA damage response pathway. Here the authors reveal how RNF168 ubiquitinates the H2A family including noncanonical variants, H2AZ and macroH2A1/2, at the divergent N-terminal tail lysine residue.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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